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7xtl
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7xtl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XTL FirstGlance]. <br> | <table><tr><td colspan='2'>[[7xtl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XTL FirstGlance]. <br> | ||
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7xtl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xtl OCA], [https://pdbe.org/7xtl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xtl RCSB], [https://www.ebi.ac.uk/pdbsum/7xtl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xtl ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.972Å</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7xtl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xtl OCA], [https://pdbe.org/7xtl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xtl RCSB], [https://www.ebi.ac.uk/pdbsum/7xtl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xtl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/MGT4A_HUMAN MGT4A_HUMAN] Glycosyltransferase that catalyze the transfer of GlcNAc from UDP-GlcNAc to the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans through a beta1-4 linkage and participates in the production of tri- and tetra-antennary N-linked sugar chains (PubMed:17006639). Involved in glucose transport by mediating SLC2A2/GLUT2 glycosylation, thereby controlling cell-surface expression of SLC2A2 in pancreatic beta cells (By similarity).[UniProtKB:Q812G0]<ref>PMID:17006639</ref> | [https://www.uniprot.org/uniprot/MGT4A_HUMAN MGT4A_HUMAN] Glycosyltransferase that catalyze the transfer of GlcNAc from UDP-GlcNAc to the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans through a beta1-4 linkage and participates in the production of tri- and tetra-antennary N-linked sugar chains (PubMed:17006639). Involved in glucose transport by mediating SLC2A2/GLUT2 glycosylation, thereby controlling cell-surface expression of SLC2A2 in pancreatic beta cells (By similarity).[UniProtKB:Q812G0]<ref>PMID:17006639</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | N-glycans are modified by glycosyltransferases in the endoplasmic reticulum and Golgi apparatus. N-acetylglucosaminyltransferase IV (GnT-IV) is a Golgi-localized glycosyltransferase that synthesizes complex-type N-glycans in vertebrates. This enzyme attaches N-acetylglucosamine (GlcNAc) to the alpha-1,3-linked mannose branch of the N-glycan core structure via a beta-1,4 linkage. Deficiency of this enzyme is known to cause abnormal cellular functions, making it a vital enzyme for living organisms. However, there has been no report on its three-dimensional structure to date. Here, we demonstrated that the C-terminal regions (named CBML) of human GnT-IVa and Bombyx mori ortholog have the ability to bind beta-N-acetylglucosamine. Additionally, we determined the crystal structures of human CBML, B. mori CBML, and its complex with beta-GlcNAc at 1.97, 1.47, and 1.15 A resolutions, respectively, and showed that they adopt a beta-sandwich fold, similar to carbohydrate-binding module family 32 (CBM32) proteins. The regions homologous to CBML (>/=24 percent identity) were found in GnT-IV isozymes, GnT-IVb, and GnT-IVc (known as GnT-VI), and the structure of B. mori CBML in complex with beta-GlcNAc indicated that the GlcNAc-binding residues were highly conserved among these isozymes. These residues are also conserved with the GlcNAc-binding CBM32 domain of beta-N-acetylhexosaminidase NagH from Clostridium perfringens despite the low sequence identity (<20 percent). Taken together with the phylogenetic analysis, these findings indicate that these CBMLs may be novel CBM family proteins with GlcNAc-binding ability. | ||
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| - | Crystal structure and sugar-binding ability of the C-terminal domain of N-acetylglucosaminyltransferase IV establish a new carbohydrate-binding module family.,Oka N, Mori S, Ikegaya M, Park EY, Miyazaki T Glycobiology. 2022 Sep 15. pii: 6700080. doi: 10.1093/glycob/cwac058. PMID:36106687<ref>PMID:36106687</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 7xtl" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of the C-terminal domain of human N-acetylglucosaminyltransferase IVa
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